2c56
From Proteopedia
(New page: 200px<br /> <applet load="2c56" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c56, resolution 2.10Å" /> '''A COMPARATIVE STUDY...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2C56 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | + | 2C56 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]] with SUC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C56 OCA]]. |
==Reference== | ==Reference== | ||
A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1., Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS, J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16306042 16306042] | A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1., Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS, J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16306042 16306042] | ||
| - | [[Category: Human herpesvirus | + | [[Category: Human herpesvirus 4]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Uridine nucleosidase]] | ||
[[Category: Baldwin, G.S.]] | [[Category: Baldwin, G.S.]] | ||
[[Category: Bellamy]] | [[Category: Bellamy]] | ||
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[[Category: uracil dna glycosylase]] | [[Category: uracil dna glycosylase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:37:27 2007'' |
Revision as of 11:32, 30 October 2007
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A COMPARATIVE STUDY OF URACIL DNA GLYCOSYLASES FROM HUMAN AND HERPES SIMPLEX VIRUS TYPE 1
Overview
Uracil-DNA glycosylase (UNG) is the key enzyme responsible for initiation, of base excision repair. We have used both kinetic and binding assays for, comparative analysis of UNG enzymes from humans and herpes simplex virus, type 1 (HSV-1). Steady-state fluorescence assays showed that hUNG has a, much higher specificity constant (k(cat)/K(m)) compared with the viral, enzyme due to a lower K(m). The binding of UNG to DNA was also studied, using a catalytically inactive mutant of UNG and non-cleavable substrate, analogs (2'-deoxypseudouridine and 2'-alpha-fluoro-2'-deoxyuridine)., Equilibrium DNA binding revealed that both human and HSV-1 UNG enzymes, bind to abasic DNA and both substrate analogs more weakly than to, uracil-containing DNA. Structure determination of HSV-1 D88N/H210N UNG in, ... [(full description)]
About this Structure
2C56 is a [Single protein] structure of sequence from [Human herpesvirus 4] with SUC as [ligand]. Active as [Uridine nucleosidase], with EC number [3.2.2.3]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
A comparative study of uracil-DNA glycosylases from human and herpes simplex virus type 1., Krusong K, Carpenter EP, Bellamy SR, Savva R, Baldwin GS, J Biol Chem. 2006 Feb 24;281(8):4983-92. Epub 2005 Nov 22. PMID:16306042
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